(data stored in ACNUC1104 zone)

SWISSPROT: B1K8U9_BURCC

ID   B1K8U9_BURCC            Unreviewed;       632 AA.
AC   B1K8U9;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   RecName: Full=Peptidoglycan D,D-transpeptidase FtsI {ECO:0000256|HAMAP-Rule:MF_02080};
DE            EC=3.4.16.4 {ECO:0000256|HAMAP-Rule:MF_02080};
DE   AltName: Full=Penicillin-binding protein 3 {ECO:0000256|HAMAP-Rule:MF_02080};
DE            Short=PBP-3 {ECO:0000256|HAMAP-Rule:MF_02080};
GN   Name=ftsI {ECO:0000256|HAMAP-Rule:MF_02080};
GN   OrderedLocusNames=Bcenmc03_3290 {ECO:0000313|EMBL:ACA92446.1};
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92446.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall
CC       at the division septum. {ECO:0000256|HAMAP-Rule:MF_02080}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02080};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02080}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02080}.
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DR   EMBL; CP000959; ACA92446.1; -; Genomic_DNA.
DR   RefSeq; WP_011547845.1; NC_010515.1.
DR   EnsemblBacteria; ACA92446; ACA92446; Bcenmc03_3290.
DR   KEGG; bcm:Bcenmc03_3290; -.
DR   HOGENOM; HOG000049554; -.
DR   KO; K03587; -.
DR   OMA; DPQIVVY; -.
DR   BioCyc; BCEN406425:G1GBC-3494-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002169; Chromosome 2.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_02080; FtsI_transpept; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR037532; FtsI_transpept.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56519; SSF56519; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1K8U9.
DR   SWISS-2DPAGE; B1K8U9.
KW   Carboxypeptidase {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002169};
KW   Glycosyltransferase {ECO:0000313|EMBL:ACA92446.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Transferase {ECO:0000313|EMBL:ACA92446.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02080}.
FT   DOMAIN       75    217       PBP_dimer. {ECO:0000259|Pfam:PF03717}.
FT   DOMAIN      259    560       Transpeptidase. {ECO:0000259|Pfam:
FT                                PF00905}.
FT   ACT_SITE    306    306       Acyl-ester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_02080}.
SQ   SEQUENCE   632 AA;  67815 MW;  0D59B09EAB1A46A6 CRC64;
     MSVKKKTHPA DPYAAATKNP MLASRLPMWR SRLIVVVVFL AFAALIARAF WVQVANQDFY
     VGQGQKRYQR TIELDAMRGR IVDRNGAMLA VSLSTYEIWA NPKQVADTDY PQIAKLLDLP
     LVEVKRRLGN DKTFVLLKRQ VDADTASRLD KLAIDGITQI ADSKRFYPEG ESAAHVVGFT
     NVEDKGQEGV ELAANARLQG TSGQREVIRD RLGRIVSDTR PLVPAQHGAT IELTIDRRIQ
     QLAFSQLKAA VIENNAVAGS VVVLDAQNGE ILALANYPTF DPNDRARLTG QQLRNRAVID
     TFEPGSTIKP LVVALSIDER KVTPNTVINT SPGTYKIGPA VIHDTSNHGS LTVSQALQKS
     SNVALAKLAL NLPAETIWNK YQEYGIGRAP ELTFPGVASG RLRGYKRWRP IEQATMAYGY
     GLSMSLLQIA QTYTAYAGDG TLHPVSLLKN GTDQQTIDAH RGHRVTSPQT AAAIRSMLEM
     AVGEGGTGRR ARVDGYRIGG KTGTARKQVG ASYAKGKYRA LFAGMAPMSN PRLIVAVMID
     EPRGKGYYGG TVAGPVFASV TSGSLQLLGV PPDAPVEPEK NAPAKAAAPQ KTVAAPKAAA
     PATATVAQKP SAQLKTAAQS SRPAPAKMAA AG
//

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